Necroptosis And Caspase 8

Description: Minimum order quantity: 1 unit of 1KIT

Description: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases including CASP3/4/6/7/9/10. [UniProt]

Description: The human CASP8 gene, whose product is also known as Caspase-8 and FLICE, encodes an interleukin-1beta converting enzyme (ICE)-related cysteine protease that is activated by the engagement of several different death receptors. It is immediately recruited to the Fas receptor once it oligomerizes, and its protease activity is crucial for the apoptotic response generated by the resulting death-inducing signaling complex (DISC). This gene contains at least 11 exons spanning approximately 30kb on human chromosome band 2q33-34. This region of chromosome 2 was previously reported as the location of the CASP10 gene, whose product is closely related to CASP8. Caspase-8 deficiency in humans is compatible with normal development and shows that the enzyme has a postnatal role in immune activation of naive lymphocytes.

Description: The human CASP8 gene, whose product is also known as Caspase-8 and FLICE, encodes an interleukin-1beta converting enzyme (ICE)-related cysteine protease that is activated by the engagement of several different death receptors. It is immediately recruited to the Fas receptor once it oligomerizes, and its protease activity is crucial for the apoptotic response generated by the resulting death-inducing signaling complex (DISC). This gene contains at least 11 exons spanning approximately 30kb on human chromosome band 2q33-34. This region of human chromosome 2 was previously reported as the location of the CASP10 gene, whose product is closely related to CASP8. Caspase-8 deficiency in humans is compatible with normal development and shows that the enzyme has a postnatal role in immune activation of naive lymphocytes.

Description: Caspase-8 is also known as CASP8, CAP4, MACH or MCH5. This gene encodes a member of the cysteine-aspartic acid protease family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.

Description: CASP8 is also known as CAP4, MACH or MCH5. This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. In addtion, this protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.

Description: Purified recombinant Human Caspase 8 protein

Description: Purified recombinant Mouse Caspase 8 protein

Description: Mouse monoclonal Caspase 8 antibody

Description: Rabbit polyclonal Caspase 8 antibody

Description: Rabbit polyclonal Caspase 8 antibody

Description: Rabbit polyclonal Caspase 8 antibody

Description: Rabbit polyclonal Caspase 8 antibody

Description: Rabbit polyclonal Caspase 8 antibody